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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

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Metabolite; its structure appears as you zoom in
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Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

EHHADH dehydrogenates 3-hydroxyhexacosanoyl-CoA

3-hydroxyhexacosanoyl-CoA + NAD+ → 3-ketohexacosanoyl-CoA + NADH + H+

Reactome: R-HSA-6809264
Compartment: peroxisomal matrix
Rhea: RHEA:78637

Inputs

3-hydroxyhexacosanoyl-CoACHEBI:76378, C47H82N7O18P3S, peroxisomal matrix
NAD+CHEBI:57540, C21H26N7O14P2, peroxisomal matrix

Outputs

3-ketohexacosanoyl-CoACHEBI:73980, C47H80N7O18P3S, peroxisomal matrix
NADHCHEBI:57945, C21H27N7O14P2, peroxisomal matrix
H+CHEBI:15378, H, peroxisomal matrix

Catalysed by

(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity of EHHADH [peroxisomal matrix]EC 1.1.1.35; UniProt Q08426

Literature

Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro Biochem. Biophys. Res. Commun., 1991
Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids J. Lipid Res., 2004
Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids J. Lipid Res., 2012
Induction, immunochemical identity and immunofluorescence localization of an 80 000-molecular-weight peroxisome-proliferation-associated polypeptide (polypeptide PPA-80) and peroxisomal enoyl-CoA hydratase of mouse liver and renal cortex Biochem. J., 1981
Peroxisomal beta oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase Biochem. Biophys. Res. Commun., 1979